Studies on Molecular Mechanism of Bioluminescence

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The three-dimensional structure of FP390 protein from a bioluminescent bacterium, Photobacterium phosphoreum, has been determined at 3 A resolution on the basis of diffraction data collected by synchrotron radiation. The crystal structure of this protein was solved by the molecular replacement procedure and refined at 2.7 A resolution to a R value of 24.0%.The remarkable feature of the structure is that two monomer molecules related by the non-crystallographic two-fold axis to form a dimeric structure. There two Q-flavin molecules in each monomer. One of them is located at the molecular surface and the another is at the dimer interface. The electron density of myristic acids of the Q-flavin at the dimer interface in both monomer are weak and unclear, showing the possibility that Q-flavins bound in this site are not a single species but a mixture of two components.